The yeast p24 complex regulates GPI-anchored protein transport and quality control by monitoring anchor remodeling

• DOI: 10.1091/mbc.e11-04-0294
• Publication Date: 2011-06-17T22:54:20Z
• Authors: Guillaume A. Cast...; Auxiliadora Aguil...; Javier Manzano-Lopez; Sharon Epstein; Kentaro Kajiwara; Kouichi Funato; Reika Watanabe; Howard Riezman; Manuel Muñiz
• Keywords: COPII; COPI; Vesicular Transport Proteins; Transport protein; Secretory protein; Lipid microdomain

Glycosylphosphatidylinositol (GPI)-anchored proteins are secretory that attached to the cell surface of eukaryotic cells by a glycolipid moiety. Once GPI anchoring has occurred in lumen endoplasmic reticulum (ER), structure lipid part on anchor undergoes remodeling process prior ER exit. In this study, we provide evidence suggesting yeast p24 complex, through binding specifically GPI-anchored an anchor-dependent manner, plays dual role their selective trafficking. First, complex promotes efficient exit remodeled after concentration connecting them with COPII coat and thus facilitates incorporation into vesicles. Second, it retrieves escaped, unremodeled from Golgi COPI Therefore sensing status anchor, regulates protein intracellular transport coordinates correct remodeling.